Ammino Acids And Proteins Flashcards
Where do humans get proteins from?
Foods: meats, eggs, diary and fish.
Where in the body are proteins found?
-Enzymes
-Hormones
-Collogen
-Antibodies
What is the polymer of proteins called?
Polypeptide
What is the monomer of proteins called?
Ammino acids
What elements do all proteins include?
O, H, C, N (sometimes S)
What groups do all proteins include in their basic structures?
-Amnio group
-Carboxyl group
-R group
What group varies in a protein structure?
R group- structure determines function.
How do humans get proteins which are not synthesised in the body?
Consuming foods which contain proteins and are then broken down into ammino acids (by hydrolysing) to then build more proteins.
What bonds are in ammino acids?
Peptide bond between carbon and nitrogen (very strong).
How many natural proteins are there?
20
How do plants absorb proteins?
Through nitrogen in the soil.
Which enzymes hydrolyses proteins?
Protease.
What does a reaction between two ammino acids from?
A dipeptide
What type of bond is a peptide bond?
Very strong covalent bond.
How are proteins produced in the body?
Produced from the mRNA to have the right sequence and therefore function (goes through the ribosomes, nucleus and the rough ER).
What is the primary structure of a protein?
A chain of ammino acids with peptide bonds.
What is the secondary structure of a protein?
-Forms an alpha helix or a beta pleated sheet.
-Formed by folding or coiling of the primary structure.
-Has hydrogen bonds between carboxyl and ammino groups- 4 places in between.
What is the tertiary structure of a protein?
-Further coiling and folding of the secondary structure.
-Has three bond: hydrogen, ionic and disulphide bridges.
-Most proteins are now functional.
What is the quaternary structure of a protein?
-Contains more than one polypeptide chain.
-Very specific
-Still coiled or pleated
-Contain inorganic compounds such as iron.
What is an example of a quaternity protein?
Haemoglobin.
Disulphide bridges:
-Very strong
-Broken down by reducing agents
-Placement is determined by R group.
-Between any ammino acid which contain S.
Hydrogen bonds:
-Broken down easily by temperature and pH as the concentration is changed.
Ionic bonds:
-Formed by oxygen on carboxyl groups.
-Between positive and negatively charged elements.
How do globular proteins form?
-Hydrophobic parts of the R group move to the centre of the polypeptide to avid water.
-Hydrophilic parts move towards the water.
-Causes twisting of the ammino acid chain and changes shape.
How is the tertiary structure denatured?
By heating
-Increases kinetic energy so parts vibrate faster.
-Bonds are broken(not covalent) and the structure begins to untwist.
What extra group does the quaternary structure have?
A prosthetic group that helps it perform its function.
What are the two types of proteins?
Globular and Fiberous.
What are the features of fibrous proteins?
-Has three polypeptide chain (triple helix)
-Has structural functions.
-Repetitive structure
-Insoluble in water
-Has hydrogen bonds.
-Has a long and thin shape
What are the features of globular proteins?
-Has 4 polypeptide chains (2 alpha, 2 beta)
-Has a spherical structure
-Functional proteins
-Soluble in water
-Has the three types of bonds
